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Histone deacetylase (EC 3.5.1.98)

 F7ENH8_RAT              Unreviewed;       488 AA.
F7ENH8;
03-APR-2013, integrated into UniProtKB/TrEMBL.
03-APR-2013, sequence version 1.
25-APR-2018, entry version 51.
RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894283};
EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894283};
Name=Hdac2 {ECO:0000313|EMBL:EDL87791.1,
ECO:0000313|Ensembl:ENSRNOP00000000742, ECO:0000313|RGD:619976};
ORFNames=rCG_19958 {ECO:0000313|EMBL:EDL87791.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000000742, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000000742, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000742,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2] {ECO:0000313|EMBL:EDL87791.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL87791.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[3] {ECO:0000313|EMBL:EDL87791.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL87791.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000213|PubMed:22673903}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[5] {ECO:0000313|Ensembl:ENSRNOP00000000742}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000742};
Ensembl;
Submitted (FEB-2012) to UniProtKB.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
{ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894227}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913,
ECO:0000256|SAAS:SAAS00894298}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
-----------------------------------------------------------------------
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EMBL; AABR07045321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH474051; EDL87791.1; -; Genomic_DNA.
RefSeq; NP_445899.1; NM_053447.1.
UniGene; Rn.1797; -.
STRING; 10116.ENSRNOP00000000742; -.
Ensembl; ENSRNOT00000000742; ENSRNOP00000000742; ENSRNOG00000000604.
GeneID; 84577; -.
KEGG; rno:84577; -.
CTD; 3066; -.
RGD; 619976; Hdac2.
eggNOG; KOG1342; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00910000144047; -.
HOVERGEN; HBG057112; -.
KO; K06067; -.
OMA; KRVCYFF; -.
OrthoDB; EOG091G067J; -.
Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-RNO-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-RNO-8943724; Regulation of PTEN gene transcription.
Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000000604; -.
GO; GO:0000785; C:chromatin; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0035098; C:ESC/E(Z) complex; ISO:RGD.
GO; GO:0000792; C:heterochromatin; ISO:RGD.
GO; GO:0000790; C:nuclear chromatin; ISO:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0016581; C:NuRD complex; ISO:RGD.
GO; GO:0005657; C:replication fork; ISO:RGD.
GO; GO:0090571; C:RNA polymerase II transcription repressor complex; ISO:RGD.
GO; GO:0016580; C:Sin3 complex; ISO:RGD.
GO; GO:0005667; C:transcription factor complex; ISO:RGD.
GO; GO:0017053; C:transcriptional repressor complex; ISO:RGD.
GO; GO:0003682; F:chromatin binding; ISO:RGD.
GO; GO:0031490; F:chromatin DNA binding; ISO:RGD.
GO; GO:0019213; F:deacetylase activity; IDA:RGD.
GO; GO:0003700; F:DNA binding transcription factor activity; ISO:RGD.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0031072; F:heat shock protein binding; IDA:RGD.
GO; GO:0004407; F:histone deacetylase activity; IMP:RGD.
GO; GO:0034739; F:histone deacetylase activity (H4-K16 specific); ISO:RGD.
GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
GO; GO:0035851; F:Krueppel-associated box domain binding; ISO:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0051059; F:NF-kappaB binding; ISO:RGD.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:RGD.
GO; GO:0033558; F:protein deacetylase activity; ISO:RGD.
GO; GO:0003723; F:RNA binding; ISO:RGD.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:RGD.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; ISO:RGD.
GO; GO:0001226; F:RNA polymerase II transcription corepressor binding; ISO:RGD.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; ISO:RGD.
GO; GO:0048149; P:behavioral response to ethanol; IEP:RGD.
GO; GO:0055013; P:cardiac muscle cell development; ISO:RGD.
GO; GO:0003300; P:cardiac muscle hypertrophy; IEP:RGD.
GO; GO:1903351; P:cellular response to dopamine; IEP:RGD.
GO; GO:0034605; P:cellular response to heat; IEP:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:RGD.
GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
GO; GO:0035984; P:cellular response to trichostatin A; ISO:RGD.
GO; GO:0032922; P:circadian regulation of gene expression; ISO:RGD.
GO; GO:0016358; P:dendrite development; ISO:RGD.
GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
GO; GO:0009913; P:epidermal cell differentiation; ISO:RGD.
GO; GO:0061029; P:eyelid development in camera-type eye; ISO:RGD.
GO; GO:0061198; P:fungiform papilla formation; ISO:RGD.
GO; GO:0060789; P:hair follicle placode formation; ISO:RGD.
GO; GO:0021766; P:hippocampus development; ISO:RGD.
GO; GO:0016575; P:histone deacetylation; IMP:RGD.
GO; GO:0070932; P:histone H3 deacetylation; IMP:RGD.
GO; GO:0070734; P:histone H3-K27 methylation; ISO:RGD.
GO; GO:0070933; P:histone H4 deacetylation; ISO:RGD.
GO; GO:0006344; P:maintenance of chromatin silencing; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISO:RGD.
GO; GO:0061000; P:negative regulation of dendritic spine development; IMP:RGD.
GO; GO:0043392; P:negative regulation of DNA binding; IMP:RGD.
GO; GO:0043433; P:negative regulation of DNA binding transcription factor activity; ISO:RGD.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
GO; GO:2000757; P:negative regulation of peptidyl-lysine acetylation; IMP:RGD.
GO; GO:1902894; P:negative regulation of pri-miRNA transcription by RNA polymerase II; ISO:RGD.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:RGD.
GO; GO:0030182; P:neuron differentiation; ISO:RGD.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; ISO:RGD.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:RGD.
GO; GO:0032732; P:positive regulation of interleukin-1 production; IMP:RGD.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:RGD.
GO; GO:0045862; P:positive regulation of proteolysis; ISO:RGD.
GO; GO:0010870; P:positive regulation of receptor biosynthetic process; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:RGD.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:RGD.
GO; GO:0006476; P:protein deacetylation; ISO:RGD.
GO; GO:0090311; P:regulation of protein deacetylation; ISO:RGD.
GO; GO:0051896; P:regulation of protein kinase B signaling; ISO:RGD.
GO; GO:0060297; P:regulation of sarcomere organization; ISO:RGD.
GO; GO:0001975; P:response to amphetamine; IEP:RGD.
GO; GO:0031000; P:response to caffeine; IEP:RGD.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0035094; P:response to nicotine; IEP:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR003084; His_deacetylse_1.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR023696; Ureohydrolase_dom_sf.
PANTHER; PTHR10625; PTHR10625; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037913; His_deacetylse_1; 1.
PRINTS; PR01270; HDASUPER.
PRINTS; PR01271; HISDACETLASE.
SUPFAM; SSF52768; SSF52768; 1.
1: Evidence at protein level;
Chromatin regulator {ECO:0000256|PIRNR:PIRNR037913,
ECO:0000256|SAAS:SAAS00894233}; Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Hydrolase {ECO:0000256|PIRNR:PIRNR037913,
ECO:0000256|SAAS:SAAS00870288};
Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
Nucleus {ECO:0000256|PIRNR:PIRNR037913,
ECO:0000256|SAAS:SAAS00894277};
Proteomics identification {ECO:0000213|PeptideAtlas:F7ENH8};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Transcription {ECO:0000256|PIRNR:PIRNR037913,
ECO:0000256|SAAS:SAAS00894290};
Transcription regulation {ECO:0000256|PIRNR:PIRNR037913,
ECO:0000256|SAAS:SAAS00894290}.
DOMAIN 29 318 Hist_deacetyl.
{ECO:0000259|Pfam:PF00850}.
COILED 444 464 {ECO:0000256|SAM:Coils}.
ACT_SITE 142 142 Proton acceptor.
{ECO:0000256|PIRSR:PIRSR037913-1}.
METAL 177 177 Divalent metal cation.
{ECO:0000256|PIRSR:PIRSR037913-3}.
METAL 179 179 Divalent metal cation.
{ECO:0000256|PIRSR:PIRSR037913-3}.
METAL 265 265 Divalent metal cation.
{ECO:0000256|PIRSR:PIRSR037913-3}.
BINDING 100 100 Substrate.
{ECO:0000256|PIRSR:PIRSR037913-2}.
BINDING 150 150 Substrate; via carbonyl oxygen.
{ECO:0000256|PIRSR:PIRSR037913-2}.
BINDING 304 304 Substrate.
{ECO:0000256|PIRSR:PIRSR037913-2}.
SEQUENCE 488 AA; 55345 MW; 35E7FCD06A2EC1AE CRC64;
MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR KMEIYRPHKA
TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED CPVFDGLFEF CQLSTGGSVA
GAVKLNRQQT DMAVNWAGGL HHAKKSEASG FCYVNDIVLA VLELLKYHQR VLYIDIDIHH
GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ
IFKPIISKVM EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG
GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN MTNQNTPEYM
EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE DPDKRISIRA SDKRIACDEE
FSDSEDEGEG GRRNVADHKK GAKKARIEED KKEAEDKRTD VKEEDKSKDN SGEKTDTKGA
KSEQLNNP


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6017 Snell Ave, Ste 357
San Jose, CA 95123




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